ID L7EQZ6_9ACTN Unreviewed; 552 AA.
AC L7EQZ6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Putative phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase {ECO:0000313|EMBL:ELP61334.1};
GN ORFNames=STRTUCAR8_06901 {ECO:0000313|EMBL:ELP61334.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP61334.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP61334.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP61334.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1. {ECO:0000256|ARBA:ARBA00004954}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004844}.
CC -!- SIMILARITY: Belongs to the PurH family.
CC {ECO:0000256|ARBA:ARBA00007667}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELP61334.1}.
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DR EMBL; AEJB01000690; ELP61334.1; -; Genomic_DNA.
DR AlphaFoldDB; L7EQZ6; -.
DR STRING; 85558.T45_01442; -.
DR PATRIC; fig|698760.3.peg.9710; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000010931; Unassembled WGS sequence.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01421; IMPCH; 1.
DR Gene3D; 3.40.140.20; -; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1.
DR PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 1.
DR Pfam; PF01808; AICARFT_IMPCHas; 1.
DR Pfam; PF02142; MGS; 1.
DR SMART; SM00798; AICARFT_IMPCHas; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ELP61334.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELP61334.1}.
FT DOMAIN 7..158
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 329..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..350
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..446
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 59064 MW; B1D37DC37B1F8624 CRC64;
MTADITVTAE SNKRALRRAL VSVYDKTGLE ELARGLHEAG VELVSTGSTA GRIAAAGVPV
TKVEELTGFP ECLDGRVKTL HPKVHAGILA DLRLEDHRTQ LAELGVEPFD LVVVNLYPFR
ETVASGASPD ECVEQIDIGG PSMVRAAAKN HPSVAVVTSP ARYADVLAAV KDGGFDLTAR
KRLAAEAFRH TAEYDIAVSS WFASVYAPAD DSPFPGFIAA ALERKSTLRY GENPHQPAAL
YVDGTGTGLA EAEQLHGKEM SYNNYTDTDA ARRAAYDHDE PCVAIIKHAN PCGIAVGSDV
AEAHRKAHAC DPLSAFGGVI TVNRPVARSW RNRSRRSSRG HRRARLRGRR PRSPRQEEEH
PRPEGPGRAL APRRGQAHRR RCAPPGDGPS PGGRRRPGQL DPGDGRGTVR GRARGTRLRL
EGVPRGQVQR HPARQGRRLG RRRHGPGQPR RLGEAGGRAG RGGAGARCVR GLGRVLPVPG
RAGDPHGGRR QGGCAARRFD ARRARGRGGA EGGRHHVLHG DAALLPLSPA SSAERHVLRP
TGIRSGGPRA FS
//
